Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Zinc/cadmium/lead-transporting P-type ATPase

Gene

zntA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Confers resistance to zinc, cadmium and lead (PubMed:9405611, PubMed:9364914, PubMed:9830000, PubMed:10660539, PubMed:17326661). Couples the hydrolysis of ATP with the export of zinc, cadmium or lead, with highest activity when the metals are present as metal-thiolate complexes (PubMed:9405611, PubMed:10660539, PubMed:17326661). Can also bind nickel, copper, cobalt and mercury (PubMed:10660539, PubMed:17326661).5 Publications

Catalytic activityi

ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out).3 Publications
ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out).3 Publications
ATP + H2O + Pb2+(In) = ADP + phosphate + Pb2+(Out).2 Publications

Enzyme regulationi

Inhibited by orthovanadate.1 Publication

Kineticsi

  1. KM=6.9 µM for Pb2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  2. KM=6.1 µM for Pb2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  3. KM=118 µM for Pb2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  4. KM=150 µM for Pb2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  5. KM=5.1 µM for Zn2+ (at 37 degrees Celsius and pH 7.0)2 Publications
  6. KM=109 µM for Zn2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  7. KM=105 µM for Zn2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  8. KM=3.1 µM for Cd2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  9. KM=115 µM for Cd2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  10. KM=123 µM for Cd2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  11. KM=3.4 µM for Cu2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  12. KM=85 µM for Cu2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  13. KM=2.1 µM for Ni2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  14. KM=169 µM for Ni2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  15. KM=4.0 µM for Co2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  16. KM=75 µM for Co2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  1. Vmax=0.88 µmol/min/mg enzyme with Pb2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  2. Vmax=0.638 µmol/min/mg enzyme with Pb2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  3. Vmax=3.02 µmol/min/mg enzyme with Pb2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  4. Vmax=2.497 µmol/min/mg enzyme with Pb2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  5. Vmax=0.19 µmol/min/mg enzyme with Zn2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  6. Vmax=0.21 µmol/min/mg enzyme with Zn2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  7. Vmax=0.96 µmol/min/mg enzyme with Zn2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  8. Vmax=0.932 µmol/min/mg enzyme with Zn2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  9. Vmax=0.102 µmol/min/mg enzyme with Cd2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  10. Vmax=1.16 µmol/min/mg enzyme with Cd2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  11. Vmax=0.862 µmol/min/mg enzyme with Cd2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  12. Vmax=0.085 µmol/min/mg enzyme with Cu2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  13. Vmax=0.104 µmol/min/mg enzyme with Cu2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  14. Vmax=0.076 µmol/min/mg enzyme with Ni2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  15. Vmax=0.138 µmol/min/mg enzyme with Ni2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  16. Vmax=0.036 µmol/min/mg enzyme with Co2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  17. Vmax=0.103 µmol/min/mg enzyme with Co2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi58Zinc 11 Publication1
Metal bindingi59Zinc 12 Publications1 Publication1
Metal bindingi62Zinc 12 Publications1 Publication1
Metal bindingi392Zinc 24 Publications1
Metal bindingi394Zinc 24 Publications1
Active sitei4364-aspartylphosphate intermediateBy similarity1
Metal bindingi436MagnesiumBy similarity1
Metal bindingi438Magnesium; via carbonyl oxygenBy similarity1
Metal bindingi628MagnesiumBy similarity1
Sitei693Important for metal transportBy similarity2 Publications1
Metal bindingi714Zinc 22 Publications1

GO - Molecular functioni

  • ATPase activity Source: EcoliWiki
  • ATP binding Source: UniProtKB-KW
  • cadmium-exporting ATPase activity Source: EcoCyc
  • cobalt ion transmembrane transporter activity Source: EcoCyc
  • lead ion transmembrane transporter activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • nickel cation transmembrane transporter activity Source: EcoCyc
  • zinc-exporting ATPase activity Source: EcoCyc

GO - Biological processi

  • cobalt ion transport Source: EcoCyc
  • detoxification of zinc ion Source: EcoliWiki
  • lead ion transport Source: EcoCyc
  • response to cadmium ion Source: EcoliWiki
  • zinc II ion transport Source: EcoliWiki

Keywordsi

Molecular functionHydrolase
Biological processIon transport, Transport, Zinc transport
LigandATP-binding, Cadmium, Lead, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:YHHO-MONOMER.
MetaCyc:YHHO-MONOMER.
SABIO-RKiP37617.

Protein family/group databases

TCDBi3.A.3.6.2. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc/cadmium/lead-transporting P-type ATPaseCurated (EC:3.6.3.-2 Publications, EC:3.6.3.33 Publications, EC:3.6.3.53 Publications)
Alternative name(s):
Pb(II)/Cd(II)/Zn(II)-translocating ATPase1 Publication
Zn(2+)/Cd(2+)/Pb(2+) export ATPaseCurated
Gene namesi
Name:zntA2 Publications
Synonyms:yhhO
Ordered Locus Names:b3469, JW3434
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12215. zntA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 124CytoplasmicCuratedAdd BLAST124
Transmembranei125 – 145HelicalSequence analysisAdd BLAST21
Topological domaini146PeriplasmicCurated1
Transmembranei147 – 167HelicalSequence analysisAdd BLAST21
Topological domaini168 – 179CytoplasmicCuratedAdd BLAST12
Transmembranei180 – 197HelicalSequence analysisAdd BLAST18
Topological domaini198 – 202PeriplasmicCurated5
Transmembranei203 – 222HelicalSequence analysisAdd BLAST20
Topological domaini223 – 356CytoplasmicCuratedAdd BLAST134
Transmembranei357 – 377HelicalSequence analysisAdd BLAST21
Topological domaini378 – 383PeriplasmicCurated6
Transmembranei384 – 404HelicalSequence analysisAdd BLAST21
Topological domaini405 – 685CytoplasmicCuratedAdd BLAST281
Transmembranei686 – 702HelicalSequence analysisAdd BLAST17
Topological domaini703 – 707PeriplasmicCurated5
Transmembranei708 – 729HelicalSequence analysisAdd BLAST22
Topological domaini730 – 732Cytoplasmic1 Publication3

GO - Cellular componenti

  • integral component of membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutant exhibits hypersensitivity to zinc, cadmium, lead and, to a lesser extent, cobalt and nickel.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi59 – 62CAAC → AAAA: 2-3-fold decrease in ATPase activity. Binds metal ion only at the transmembrane site. 1 Publication4
Mutagenesisi59 – 62CAAC → SAAS: Reduces the ATPase activity by 50%. Reduces level of phosphorylation. 1 Publication4
Mutagenesisi392 – 394CPC → APA: Lack of ATPase activity. Binds metal ion only at the N-terminal site. 1 Publication3
Mutagenesisi392 – 394CPC → SPS: Lack of ATPase activity. Loss of zinc-stimulated phosphorylation. 1 Publication3
Mutagenesisi392C → A: Lack of activity. Cannot bind metal at the transmembrane site. Lack of phosphorylation with ATP. 1 Publication1
Mutagenesisi392C → H or S: Decrease in activity. Binds Zn(2+), Cd(2+), Ni(2+), Co(2+) and Cu(2+), but not Pb(2+). 1 Publication1
Mutagenesisi393P → A: Lack of activity with any metal. Cannot bind metal at the transmembrane site. Lack of phosphorylation with ATP. 1 Publication1
Mutagenesisi394C → A: Lack of activity. Cannot bind metal at the transmembrane site. Lack of phosphorylation with ATP. 1 Publication1
Mutagenesisi394C → H or S: Decrease in activity. Binds Zn(2+), Cd(2+), Ni(2+), Co(2+) and Cu(2+), but not Pb(2+). 1 Publication1
Mutagenesisi693K → N: Loss of zinc-stimulated ATPase activity. Poorly phosphorylated with ATP. 1 Publication1
Mutagenesisi714D → M: Shows high metal-independent ATPase activity. Poorly phosphorylated with ATP. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000463321 – 732Zinc/cadmium/lead-transporting P-type ATPaseAdd BLAST732

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP37617.
PaxDbiP37617.
PRIDEiP37617.

Expressioni

Inductioni

Induced by zinc.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4262921. 11 interactors.
DIPiDIP-12947N.
IntActiP37617. 8 interactors.
MINTiMINT-1256950.
STRINGi316385.ECDH10B_3643.

Structurei

Secondary structure

1732
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 56Combined sources9
Helixi62 – 71Combined sources10
Beta strandi73 – 82Combined sources10
Turni83 – 86Combined sources4
Beta strandi87 – 94Combined sources8
Helixi97 – 107Combined sources11
Beta strandi110 – 113Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MWYNMR-A46-118[»]
1MWZNMR-A46-118[»]
ProteinModelPortaliP37617.
SMRiP37617.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37617.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini49 – 113HMAPROSITE-ProRule annotationAdd BLAST65

Domaini

Has two high-affinity metal-binding sites, one in the N-terminal region and another in the transmembrane region. Both sites are able to access and bind metal ion independently of each other. The N-terminal metal-binding site is not strictly necessary for activity and metal selectivity, but is needed for maximal activity and may be involved in regulation. The metal-binding site in the transmembrane region is essential for activity of the pump.3 Publications

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C59. Bacteria.
COG2217. LUCA.
HOGENOMiHOG000250399.
InParanoidiP37617.
KOiK01534.
PhylomeDBiP37617.

Family and domain databases

CDDicd00371. HMA. 1 hit.
Gene3Di3.40.1110.10. 1 hit.
3.40.50.1000. 1 hit.
InterProiView protein in InterPro
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
PfamiView protein in Pfam
PF00403. HMA. 1 hit.
PRINTSiPR00120. HATPASE.
SUPFAMiSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
SSF81653. SSF81653. 1 hit.
SSF81665. SSF81665. 3 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiView protein in PROSITE
PS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P37617-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSTPT LSENVSGTRY
60 70 80 90 100
SWKVSGMDCA ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV
110 120 130 140 150
ESALQKAGYS LRDEQAAEEP QASRLKENLP LITLIVMMAI SWGLEQFNHP
160 170 180 190 200
FGQLAFIATT LVGLYPIARQ ALRLIKSGSY FAIETLMSVA AIGALFIGAT
210 220 230 240 250
AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT RLRKGEREEV
260 270 280 290 300
AINSLRPGDV IEVAAGGRLP ADGKLLSPFA SFDESALTGE SIPVERATGD
310 320 330 340 350
KVPAGATSVD RLVTLEVLSE PGASAIDRIL KLIEEAEERR APIERFIDRF
360 370 380 390 400
SRIYTPAIMA VALLVTLVPP LLFAASWQEW IYKGLTLLLI GCPCALVIST
410 420 430 440 450
PAAITSGLAA AARRGALIKG GAALEQLGRV TQVAFDKTGT LTVGKPRVTA
460 470 480 490 500
IHPATGISES ELLTLAAAVE QGATHPLAQA IVREAQVAEL AIPTAESQRA
510 520 530 540 550
LVGSGIEAQV NGERVLICAA GKHPADAFTG LINELESAGQ TVVLVVRNDD
560 570 580 590 600
VLGVIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE
610 620 630 640 650
FKAGLLPEDK VKAVTELNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD
660 670 680 690 700
VALETADAAL THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT
710 720 730
LLGMTGLWLA VLADTGATVL VTANALRLLR RR
Length:732
Mass (Da):76,840
Last modified:October 1, 1994 - v1
Checksum:i25476EA830786465
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18444.1.
U00096 Genomic DNA. Translation: AAC76494.1.
AP009048 Genomic DNA. Translation: BAE77824.1.
PIRiS47688.
RefSeqiNP_417926.1. NC_000913.3.
WP_000106551.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76494; AAC76494; b3469.
BAE77824; BAE77824; BAE77824.
GeneIDi947972.
KEGGiecj:JW3434.
eco:b3469.
PATRICifig|1411691.4.peg.3256.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiZNTA_ECOLI
AccessioniPrimary (citable) accession number: P37617
Secondary accession number(s): Q2M7D2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 5, 2017
This is version 164 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families